Research workbench
A4V mutant of human SOD1 with ebselen derivative 1
Analyse A4V mutant of human SOD1 with ebselen derivative 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SPJ
- Type
- protein
- Length
- 916 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00441
- Ligands
- LR2, ZN, SO4, CL
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, I, J | — | protein | 153 | — | P00441 |
| E, F | — | protein | 152 | — | P00441 |
Ligands and binding sites
- LR2 · ~{N}-pyridin-2-yl-2-selanyl-benzamide · ligand · 6 copies · chains A, B, E, F, I, J
- ZN · Zinc ion · metal · 12 copies · chains A, B, E, F, I, J
- SO4 · Sulfate ion · ion · 30 copies · chains A, B, E, F, I, J
- CL · Chloride ion · ion · 6 copies · chains A, I, B, E, F, J
- DMS · Dimethyl sulfoxide · additive · 9 copies · chains A, B, E, I, J
- GOL · Glycerol · additive · 6 copies · chains A, B, E, F, I, J
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6SPJ · A4V mutant of human SOD1 with ebselen derivative 1 · the same entry in another collection · chain J against J, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P00441
- Elsewhere: RCSB PDB 6SPJ · PDBe 6SPJ · UniProt P00441
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